Figure 6: Spatial arrangement of amino acid residues with largest contribution to the binding energy at the binding pocket. (A) Salt bridge between Asp110 side chain and the tertiary amine at pyrrolidine ring. A repulsive interaction with Cys114 is related with the presence of a chloride substituent in the aromatic ring. Orientation of the optimized hydrogen atom in (O7)H in the direction of oxygen in the hydroxyl group (O14) indicates the formation of a pseudoring. (B) Ile183 is the second closest residue to eticlopride and interacts via hydrogen and van der walls bonds. (C) Attractive interactions of Phe345 and Phe346 and repulsive contribution of Ser182. (D) Val82 repels eticlopride probably due to its interaction with region i. Yellow dashed lines show the distance of the most relevant amino acid residues to the closest atoms of eticlopride.